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Database: UniProt
Entry: H6L1B7_SAPGL
LinkDB: H6L1B7_SAPGL
Original site: H6L1B7_SAPGL 
ID   H6L1B7_SAPGL            Unreviewed;       621 AA.
AC   H6L1B7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461, ECO:0000256|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800, ECO:0000256|HAMAP-Rule:MF_00129};
GN   Name=mnmG {ECO:0000256|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129,
GN   ECO:0000313|EMBL:AFC23458.1};
GN   OrderedLocusNames=SGRA_0719 {ECO:0000313|EMBL:AFC23458.1};
OS   Saprospira grandis (strain Lewin).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC   Saprospira.
OX   NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC23458.1, ECO:0000313|Proteomes:UP000007519};
RN   [1] {ECO:0000313|EMBL:AFC23458.1, ECO:0000313|Proteomes:UP000007519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lewin {ECO:0000313|EMBL:AFC23458.1,
RC   ECO:0000313|Proteomes:UP000007519};
RX   PubMed=22675601; DOI=10.4056/sigs.2445005;
RA   Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT   "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT   a predatory marine bacterium.";
RL   Stand. Genomic Sci. 6:84-93(2012).
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC       certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
CC       {ECO:0000256|ARBA:ARBA00003717, ECO:0000256|HAMAP-Rule:MF_00129}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_00129};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000256|ARBA:ARBA00025948, ECO:0000256|HAMAP-Rule:MF_00129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000256|ARBA:ARBA00007653,
CC       ECO:0000256|HAMAP-Rule:MF_00129}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00129}.
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DR   EMBL; CP002831; AFC23458.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6L1B7; -.
DR   STRING; 984262.SGRA_0719; -.
DR   KEGG; sgn:SGRA_0719; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_10; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 9815560at2; -.
DR   Proteomes; UP000007519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR   Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR049312; GIDA_C_N.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR047001; MnmG_C_subdom.
DR   InterPro; IPR044920; MnmG_C_subdom_sf.
DR   InterPro; IPR040131; MnmG_N.
DR   NCBIfam; TIGR00136; gidA; 1.
DR   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   Pfam; PF21680; GIDA_C_1st; 1.
DR   SMART; SM01228; GIDA_assoc_3; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00129};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_00129};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00129};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007519};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00129}.
FT   DOMAIN          546..617
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   BINDING         12..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         271..285
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   621 AA;  69517 MW;  CB45124A1CA61BEF CRC64;
     MIFDTYDVVV VGAGHAGCEA AVAAANLGAK VMLATMNMET IAKMSCNPAM GGVAKGQIVR
     EIDALNGYSG IVTDHTMIQF RLLNRSKGPA MWSPRAQSDR MRFAEKWRLM LEAHPNIDFW
     QEMVTGIVVK DKKAVGIRTS LGLEIPAKTV ILTNGTFLNG LIHIGEKQMG GGRAGERAAK
     GITEQLVELG FEASRMKTGT PPRIDARSIN WSALEVQEGD QPAGKFSYTD TPELKEQRPC
     HIGYTNKKVH ECLKEGFSRS PMFNGRIQGL GPRYCPSIED KIDRFSERDR HQLFVEPEGW
     NTAEIYLNGF SSSLPEDVQF KAMRLIPGFE QAKMFRPGYA IEYDFFQPTQ LKQTLETRLV
     DGLYFAGQIN GTTGYEEAAC QGLMAGINAI RKVREEEPFV LKRSDAYIGV LIDDLINKGT
     NEPYRMFTSR AEYRILLRQD NADIRLTPIA QALGMDVEER MQRVRAKEAA ERDISEFMKS
     YSVRPEAINS YLDSLGSAPL RQPVKLMKVL LRPKVNAEAL AEHLPELKAV LDQYPKEFVE
     YSEIKAKYAG YIKKEEEQVE KMNRLESVRL PENFNYHAIQ GLSAEGQEKL SRIRPGSIGQ
     ASRISGVSAS DISILLVYMG R
//
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